Stability to proteolytic degradation in the digestive tract is considered a general feature shared by most food allergens. Current digestibility models exclusively utilize purified allergen proteins, neglecting the relevant effects of matrix that occur for foodstuff systems. In the present study, we investigated digestion stability of the major peanut allergens directly in the natural matrix using an in vitro static model that simulates the gastrointestinal digestion including the oral, gastric, duodenal and intestinal (brush border membrane enzymes) phases. Immunogenicity was evaluated by Western Blot using N=8 pooled sera of peanut allergic pediatric subjects. Immunoreactive, large-sized and fragments of Ara h 2, Ara h 6 and Ara h 3 survived hydrolysis as assessed by SDS-PAGE. Smaller resistant peptides mainly arising from Ara h 3 and also Ara h 1 were detected and further identified by LC-high resolution-MS/MS. RP-HPLC purification followed by dot-blot analysis and MS/MS-based identification demonstrated that stable IgE-binding peptides derived from Ara h 3. These results provide a more realistic picture of the potentially allergenic determinants of peanuts that survived the human digestion, taking into account the role of the food matrix, which may significantly affect gastrointestinal breakdown of peanut allergens.

Peanut digestome: Identification of digestion resistant IgE binding peptides / DI STASIO, Luigia; Picariello, Gianluca; Mongiello, Mariantonietta; Nocerino, Rita; BERNI CANANI, Roberto; Bavaro, Simona; Monaci, Linda; Ferranti, Pasquale; Mamone, Gianfranco. - In: FOOD AND CHEMICAL TOXICOLOGY. - ISSN 1873-6351. - (2017), pp. 88-98. [10.1016/j.fct.2017.06.029]

Peanut digestome: Identification of digestion resistant IgE binding peptides

DI STASIO, LUIGIA;PICARIELLO, Gianluca;NOCERINO, RITA;BERNI CANANI, ROBERTO;FERRANTI, PASQUALE;
2017

Abstract

Stability to proteolytic degradation in the digestive tract is considered a general feature shared by most food allergens. Current digestibility models exclusively utilize purified allergen proteins, neglecting the relevant effects of matrix that occur for foodstuff systems. In the present study, we investigated digestion stability of the major peanut allergens directly in the natural matrix using an in vitro static model that simulates the gastrointestinal digestion including the oral, gastric, duodenal and intestinal (brush border membrane enzymes) phases. Immunogenicity was evaluated by Western Blot using N=8 pooled sera of peanut allergic pediatric subjects. Immunoreactive, large-sized and fragments of Ara h 2, Ara h 6 and Ara h 3 survived hydrolysis as assessed by SDS-PAGE. Smaller resistant peptides mainly arising from Ara h 3 and also Ara h 1 were detected and further identified by LC-high resolution-MS/MS. RP-HPLC purification followed by dot-blot analysis and MS/MS-based identification demonstrated that stable IgE-binding peptides derived from Ara h 3. These results provide a more realistic picture of the potentially allergenic determinants of peanuts that survived the human digestion, taking into account the role of the food matrix, which may significantly affect gastrointestinal breakdown of peanut allergens.
2017
Peanut digestome: Identification of digestion resistant IgE binding peptides / DI STASIO, Luigia; Picariello, Gianluca; Mongiello, Mariantonietta; Nocerino, Rita; BERNI CANANI, Roberto; Bavaro, Simona; Monaci, Linda; Ferranti, Pasquale; Mamone, Gianfranco. - In: FOOD AND CHEMICAL TOXICOLOGY. - ISSN 1873-6351. - (2017), pp. 88-98. [10.1016/j.fct.2017.06.029]
File in questo prodotto:
File Dimensione Formato  
Peanut digestome Identification of digestion resistant IgE binding peptides.pdf

accesso aperto

Tipologia: Documento in Post-print
Licenza: Dominio pubblico
Dimensione 759.37 kB
Formato Adobe PDF
759.37 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/678631
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 43
  • ???jsp.display-item.citation.isi??? 36
social impact